PAR15_HUMAN
ID PAR15_HUMAN Reviewed; 678 AA.
AC Q460N3; J3KR47; Q8N1K3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP15 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25635049};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 7 {ECO:0000303|PubMed:20106667};
DE Short=ARTD7 {ECO:0000303|PubMed:20106667};
DE AltName: Full=B-aggressive lymphoma protein 3 {ECO:0000303|PubMed:15489334};
DE AltName: Full=Poly [ADP-ribose] polymerase 15;
DE Short=PARP-15;
GN Name=PARP15 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:26876};
GN Synonyms=BAL3 {ECO:0000303|PubMed:15489334};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-678 (ISOFORM 1), AND FUNCTION.
RX PubMed=16061477; DOI=10.1074/jbc.m505408200;
RA Aguiar R.C.T., Takeyama K., He C., Kreinbrink K., Shipp M.A.;
RT "B-aggressive lymphoma family proteins have unique domains that modulate
RT transcription and exhibit poly(ADP-ribose) polymerase activity.";
RL J. Biol. Chem. 280:33756-33765(2005).
RN [5]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [6]
RP FUNCTION.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 481-678.
RX PubMed=22823910; DOI=10.1021/jm300746d;
RA Andersson C.D., Karlberg T., Ekblad T., Lindgren A.E., Thorsell A.G.,
RA Spjut S., Uciechowska U., Niemiec M.S., Wittung-Stafshede P., Weigelt J.,
RA Elofsson M., Schuler H., Linusson A.;
RT "Discovery of ligands for ADP-ribosyltransferases via docking-based virtual
RT screening.";
RL J. Med. Chem. 55:7706-7718(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 295-470 IN COMPLEX WITH
RP SUBSTRATE.
RX PubMed=23473667; DOI=10.1016/j.str.2012.12.019;
RA Forst A.H., Karlberg T., Herzog N., Thorsell A.G., Gross A., Feijs K.L.,
RA Verheugd P., Kursula P., Nijmeijer B., Kremmer E., Kleine H.,
RA Ladurner A.G., Schuler H., Luscher B.;
RT "Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8
RT macrodomains.";
RL Structure 21:462-475(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 481-678, FUNCTION, AND
RP MUTAGENESIS OF HIS-559; GLY-560 AND TYR-604.
RX PubMed=25635049; DOI=10.1074/jbc.m114.630160;
RA Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
RA Schuler H.;
RT "Structural basis for lack of ADP-ribosyltransferase activity in poly(ADP-
RT ribose) polymerase-13/zinc finger antiviral protein.";
RL J. Biol. Chem. 290:7336-7344(2015).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins (PubMed:16061477, PubMed:25043379,
CC PubMed:25635049). Acts as a negative regulator of transcription
CC (PubMed:16061477). {ECO:0000269|PubMed:16061477,
CC ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25635049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000305};
CC -!- INTERACTION:
CC Q460N3-2; Q8IXM6: NRM; NbExp=3; IntAct=EBI-17287327, EBI-10262547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16061477}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q460N3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q460N3-2; Sequence=VSP_020971, VSP_020972;
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY64451.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK097916; BAC05197.1; -; mRNA.
DR EMBL; BC101703; AAI01704.1; -; mRNA.
DR EMBL; BC101701; AAI01702.1; -; mRNA.
DR EMBL; AC092908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ063586; AAY64451.1; ALT_INIT; mRNA.
DR CCDS; CCDS3016.1; -. [Q460N3-2]
DR CCDS; CCDS46893.1; -. [Q460N3-1]
DR RefSeq; NP_001106995.1; NM_001113523.2. [Q460N3-1]
DR RefSeq; NP_001295249.1; NM_001308320.1.
DR RefSeq; NP_689828.1; NM_152615.2. [Q460N3-2]
DR PDB; 3BLJ; X-ray; 2.20 A; A/B=481-678.
DR PDB; 3GEY; X-ray; 2.20 A; A/B/C/D=481-678.
DR PDB; 3V2B; X-ray; 2.20 A; A=295-470.
DR PDB; 4F0E; X-ray; 2.40 A; A/B/C/D=481-678.
DR PDB; 6EK3; X-ray; 1.60 A; A/B=481-678.
DR PDB; 6RY4; X-ray; 1.95 A; A/B=482-678.
DR PDB; 7OQQ; X-ray; 2.00 A; A/B=481-678.
DR PDB; 7OSP; X-ray; 1.44 A; A/B=481-678.
DR PDB; 7OSS; X-ray; 1.50 A; A/B=481-678.
DR PDB; 7OSX; X-ray; 1.60 A; A/B=481-678.
DR PDB; 7OTF; X-ray; 1.30 A; A/B=481-678.
DR PDB; 7OTH; X-ray; 1.70 A; A/B=481-678.
DR PDB; 7OUW; X-ray; 1.60 A; A/B=481-678.
DR PDB; 7OUX; X-ray; 1.95 A; A/B=481-678.
DR PDBsum; 3BLJ; -.
DR PDBsum; 3GEY; -.
DR PDBsum; 3V2B; -.
DR PDBsum; 4F0E; -.
DR PDBsum; 6EK3; -.
DR PDBsum; 6RY4; -.
DR PDBsum; 7OQQ; -.
DR PDBsum; 7OSP; -.
DR PDBsum; 7OSS; -.
DR PDBsum; 7OSX; -.
DR PDBsum; 7OTF; -.
DR PDBsum; 7OTH; -.
DR PDBsum; 7OUW; -.
DR PDBsum; 7OUX; -.
DR AlphaFoldDB; Q460N3; -.
DR SMR; Q460N3; -.
DR BioGRID; 127917; 3.
DR IntAct; Q460N3; 1.
DR STRING; 9606.ENSP00000417214; -.
DR BindingDB; Q460N3; -.
DR ChEMBL; CHEMBL2176778; -.
DR DrugBank; DB08348; N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE.
DR DrugCentral; Q460N3; -.
DR iPTMnet; Q460N3; -.
DR PhosphoSitePlus; Q460N3; -.
DR BioMuta; PARP15; -.
DR DMDM; 116248564; -.
DR MassIVE; Q460N3; -.
DR MaxQB; Q460N3; -.
DR PaxDb; Q460N3; -.
DR PeptideAtlas; Q460N3; -.
DR PRIDE; Q460N3; -.
DR ProteomicsDB; 61928; -. [Q460N3-1]
DR ProteomicsDB; 61929; -. [Q460N3-2]
DR Antibodypedia; 32915; 34 antibodies from 19 providers.
DR DNASU; 165631; -.
DR Ensembl; ENST00000310366.8; ENSP00000308436.4; ENSG00000173200.13. [Q460N3-2]
DR Ensembl; ENST00000464300.7; ENSP00000417214.2; ENSG00000173200.13. [Q460N3-1]
DR GeneID; 165631; -.
DR KEGG; hsa:165631; -.
DR MANE-Select; ENST00000464300.7; ENSP00000417214.2; NM_001113523.3; NP_001106995.1.
DR UCSC; uc003efm.3; human. [Q460N3-1]
DR CTD; 165631; -.
DR DisGeNET; 165631; -.
DR GeneCards; PARP15; -.
DR HGNC; HGNC:26876; PARP15.
DR HPA; ENSG00000173200; Group enriched (bone marrow, intestine, lymphoid tissue).
DR MIM; 612066; gene.
DR neXtProt; NX_Q460N3; -.
DR OpenTargets; ENSG00000173200; -.
DR PharmGKB; PA134905094; -.
DR VEuPathDB; HostDB:ENSG00000173200; -.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000163672; -.
DR InParanoid; Q460N3; -.
DR OMA; SQQIMAN; -.
DR OrthoDB; 681829at2759; -.
DR PhylomeDB; Q460N3; -.
DR TreeFam; TF316072; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q460N3; -.
DR SignaLink; Q460N3; -.
DR BioGRID-ORCS; 165631; 11 hits in 1078 CRISPR screens.
DR EvolutionaryTrace; Q460N3; -.
DR GenomeRNAi; 165631; -.
DR Pharos; Q460N3; Tchem.
DR PRO; PR:Q460N3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q460N3; protein.
DR Bgee; ENSG00000173200; Expressed in spleen and 89 other tissues.
DR ExpressionAtlas; Q460N3; baseline and differential.
DR Genevisible; Q460N3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IMP:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:UniProtKB.
DR Gene3D; 3.40.220.10; -; 2.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR034401; PARP15.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR PANTHER; PTHR14453:SF89; PTHR14453:SF89; 2.
DR Pfam; PF01661; Macro; 2.
DR Pfam; PF00644; PARP; 1.
DR SMART; SM00506; A1pp; 2.
DR SUPFAM; SSF52949; SSF52949; 2.
DR PROSITE; PS51154; MACRO; 2.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..678
FT /note="Protein mono-ADP-ribosyltransferase PARP15"
FT /id="PRO_0000252436"
FT DOMAIN 78..267
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 293..464
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 482..678
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312..313
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT BINDING 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT BINDING 409..413
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23473667,
FT ECO:0007744|PDB:3V2B"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020971"
FT VAR_SEQ 235..256
FT /note="RPITSPLQEVHFLVYTNDDEGC -> MLQRIGLIFLHNIVVVSNCFYF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020972"
FT VARIANT 337
FT /note="R -> K (in dbSNP:rs6793271)"
FT /id="VAR_027862"
FT VARIANT 521
FT /note="A -> T (in dbSNP:rs34383355)"
FT /id="VAR_056658"
FT VARIANT 628
FT /note="G -> R (in dbSNP:rs12489170)"
FT /id="VAR_027863"
FT MUTAGEN 559
FT /note="H->Y: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:25635049"
FT MUTAGEN 560
FT /note="G->A: Slightly reduces catalytic activity. Abolishes
FT activity; when associated with Y-559 and C-604."
FT /evidence="ECO:0000269|PubMed:25635049"
FT MUTAGEN 604
FT /note="Y->C: Reduces catalytic activity 20-fold. Abolishes
FT activity; when associated with Y-559 and A-560."
FT /evidence="ECO:0000269|PubMed:25635049"
FT CONFLICT 42
FT /note="V -> M (in Ref. 4; AAY64451)"
FT /evidence="ECO:0000305"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 370..379
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 417..434
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:3V2B"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:3V2B"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:7OTF"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:7OTF"
FT HELIX 531..548
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:7OTF"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:7OTF"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:7OTF"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:7OTH"
FT STRAND 588..595
FT /evidence="ECO:0007829|PDB:7OTF"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:7OTF"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 613..620
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:7OSX"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:7OTF"
FT STRAND 667..677
FT /evidence="ECO:0007829|PDB:7OTF"
SQ SEQUENCE 678 AA; 74576 MW; E299386DA4B2BF8C CRC64;
MAAPGPLPAA ALSPGAPTPR ELMHGVAGVT SRAGRDREAG SVLPAGNRGA RKASRRSSSR
SMSRDNKFSK KDCLSIRNVV ASIQTKEGLN LKLISGDVLY IWADVIVNSV PMNLQLGGGP
LSRAFLQKAG PMLQKELDDR RRETEEKVGN IFMTSGCNLD CKAVLHAVAP YWNNGAETSW
QIMANIIKKC LTTVEVLSFS SITFPMIGTG SLQFPKAVFA KLILSEVFEY SSSTRPITSP
LQEVHFLVYT NDDEGCQAFL DEFTNWSRIN PNKARIPMAG DTQGVVGTVS KPCFTAYEMK
IGAITFQVAT GDIATEQVDV IVNSTARTFN RKSGVSRAIL EGAGQAVESE CAVLAAQPHR
DFIITPGGCL KCKIIIHVPG GKDVRKTVTS VLEECEQRKY TSVSLPAIGT GNAGKNPITV
ADNIIDAIVD FSSQHSTPSL KTVKVVIFQP ELLNIFYDSM KKRDLSASLN FQSTFSMTTC
NLPEHWTDMN HQLFCMVQLE PGQSEYNTIK DKFTRTCSSY AIEKIERIQN AFLWQSYQVK
KRQMDIKNDH KNNERLLFHG TDADSVPYVN QHGFNRSCAG KNAVSYGKGT YFAVDASYSA
KDTYSKPDSN GRKHMYVVRV LTGVFTKGRA GLVTPPPKNP HNPTDLFDSV TNNTRSPKLF
VVFFDNQAYP EYLITFTA
